The Administrative Core of the Program Project, Structure and Funcfion of DNA Repair Enzymes, will be responsible for coordinating all of the administrative aspects of the program and for facilitating interactions among the Project and Core Directors, Senior Investigators, and their laboratory members. The overall goal is to insure the successful conduct of the research proposed in this application. The management of the DNA Repair Program will be coordinated by the Principal Investigator/Administrative Core Director, Dr. Susan Wallace, with an Executive Committee comprised of Drs. Bond, Doubli6, Morrical, Pederson and Sweasy. Specifically the aims ofthe Core are:
Aim 1. To provide administrative support for the Projects and Cores A and B, Aim 2. To monitor the scientific progress of the Projects by facilitafing monthly meefings of the Program Project participants.
Aim 3. To facilitate meefings with the External and Internal Advisory Boards.

Public Health Relevance

The studies resulfing from this Program will provide insight into how the BER and RAD51 variants in the in the normal population and in tumors may contribute to altereed DNA repair capacity. Hence, this project will both contribute to our understanding of laasic cancer biology and may provide the basis for new approaches to cancer therapy.

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Program Projects (P01)
Project #
2P01CA098993-06A1
Application #
7992630
Study Section
Special Emphasis Panel (ZCA1-RPRB-0 (M1))
Project Start
2010-07-01
Project End
2015-06-30
Budget Start
2010-07-01
Budget End
2011-08-31
Support Year
6
Fiscal Year
2010
Total Cost
$52,291
Indirect Cost
Name
University of Vermont & St Agric College
Department
Type
DUNS #
066811191
City
Burlington
State
VT
Country
United States
Zip Code
05405
Maher, R L; Marsden, C G; Averill, A M et al. (2017) Human cells contain a factor that facilitates the DNA glycosylase-mediated excision of oxidized bases from occluded sites in nucleosomes. DNA Repair (Amst) 57:91-97
Marsden, Carolyn G; Dragon, Julie A; Wallace, Susan S et al. (2017) Base Excision Repair Variants in Cancer. Methods Enzymol 591:119-157
Galick, Heather A; Marsden, Carolyn G; Kathe, Scott et al. (2017) The NEIL1 G83D germline DNA glycosylase variant induces genomic instability and cellular transformation. Oncotarget 8:85883-85895
Robey-Bond, Susan M; Benson, Meredith A; Barrantes-Reynolds, Ramiro et al. (2017) Probing the activity of NTHL1 orthologs by targeting conserved amino acid residues. DNA Repair (Amst) 53:43-51
Cannan, Wendy J; Rashid, Ishtiaque; Tomkinson, Alan E et al. (2017) The Human Ligase III?-XRCC1 Protein Complex Performs DNA Nick Repair after Transient Unwrapping of Nucleosomal DNA. J Biol Chem 292:5227-5238
Silva, Michelle C; Bryan, Katie E; Morrical, Milagros D et al. (2017) Defects in recombination activity caused by somatic and germline mutations in the multimerization/BRCA2 binding region of human RAD51 protein. DNA Repair (Amst) 60:64-76
Zhou, Jia; Chan, Jany; Lambelé, Marie et al. (2017) NEIL3 Repairs Telomere Damage during S Phase to Secure Chromosome Segregation at Mitosis. Cell Rep 20:2044-2056
Prakash, Aishwarya; Moharana, Kedar; Wallace, Susan S et al. (2017) Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase. Nucleic Acids Res 45:2897-2909
Lee, Andrea J; Wallace, Susan S (2017) Hide and seek: How do DNA glycosylases locate oxidatively damaged DNA bases amidst a sea of undamaged bases? Free Radic Biol Med 107:170-178
Lee, Andrea J; Wallace, Susan S (2016) Visualizing the Search for Radiation-damaged DNA Bases in Real Time. Radiat Phys Chem Oxf Engl 1993 128:126-133

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